WNT8B_XENLA
ID WNT8B_XENLA Reviewed; 428 AA.
AC P31291;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein Wnt-8b;
DE Short=XWnt-8b;
DE Flags: Precursor;
GN Name=wnt8b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7635061; DOI=10.1242/dev.121.7.2177;
RA Cui Y., Brown J.D., Moon R.T., Christian J.L.;
RT "Xwnt-8b: a maternally expressed Xenopus Wnt gene with a potential role in
RT establishing the dorsoventral axis.";
RL Development 121:2177-2186(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 278-390.
RX PubMed=1408135;
RA Wolda S.L., Moon R.T.;
RT "Cloning and developmental expression in Xenopus laevis of seven additional
RT members of the Wnt family.";
RL Oncogene 7:1941-1947(1992).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Plays a role in the initiation of dorsal axis
CC development. May activate a Nieuwkoop center-like signaling pathway.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P31291-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P31291-2; Sequence=VSP_006795;
CC -!- TISSUE SPECIFICITY: In adults, in brain.
CC -!- DEVELOPMENTAL STAGE: The short form increases from the onset of
CC gastrulation to swimming tadpoles and the longer form appears at the
CC end of gastrulation, is present throughout the tailbud stages and then
CC decline in tadpoles.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors (By similarity). Depalmitoleoylation leads to Wnt signaling
CC pathway inhibition (By similarity). {ECO:0000250|UniProtKB:P28026,
CC ECO:0000250|UniProtKB:P56704}.
CC -!- PTM: Proteolytic processing by tiki1 and tiki2 promotes oxidation and
CC formation of large disulfide-bond oligomers, leading to inactivation of
CC wnt8b. {ECO:0000250|UniProtKB:P28026}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; U22173; AAC59693.1; -; mRNA.
DR EMBL; L07536; AAA49989.1; -; mRNA.
DR PIR; I51680; I51680.
DR RefSeq; NP_001083754.1; NM_001090285.1. [P31291-1]
DR AlphaFoldDB; P31291; -.
DR SMR; P31291; -.
DR GeneID; 399098; -.
DR KEGG; xla:399098; -.
DR CTD; 399098; -.
DR Xenbase; XB-GENE-866182; wnt8b.S.
DR OrthoDB; 618621at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 399098; Expressed in brain and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:BHF-UCL.
DR GO; GO:0048263; P:determination of dorsal identity; IMP:BHF-UCL.
DR GO; GO:0007369; P:gastrulation; IEP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR034311; Protein_Wnt-8B.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013301; Wnt8.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF94; PTHR12027:SF94; 1.
DR Pfam; PF00110; wnt; 2.
DR PRINTS; PR01892; WNT8PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome;
KW Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..428
FT /note="Protein Wnt-8b"
FT /id="PRO_0000041453"
FT LIPID 259
FT /note="O-palmitoleoyl serine"
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..65
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 177..185
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 187..205
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 253..267
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 255..262
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..367
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 345..360
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 364..406
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 382..397
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 384..394
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 389..390
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 81..153
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_006795"
FT CONFLICT 293
FT /note="L -> P (in Ref. 2; AAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="E -> D (in Ref. 2; AAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="K -> E (in Ref. 2; AAA49989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 47586 MW; BB3F635E2B8B4744 CRC64;
MFYTGSFWFI FFILPAIPFC HSWSVNNFLM TGPKAYLIYS SSVAAGAQSG IEECKYQFAW
DKWNCPERTL QLSSHSGLRS DLNIHSTGAS PAGSGLYDTG PTSPVWSINF NRILFSRLES
HFNKTFLSRL QIPFPQGHTV QSATSLSTGF LSPANRETAF VHAISYAGVM YTLTRNCSLG
DFDNCGCDDS RNGQLGGQGW LWGGCSDNVG FGETISKQFV DPLETGQDAR AAMNLHNNEA
GRKAVKSTMK RTCKCHGVSG SCTTQTCWLQ LPEFREVGNY LKEKYHKALK VDLFHGAGNS
AASRGAIAET FRSISKKEIV HLEDSPDYCL ENKTLGLLGT EGRECLKRGK ALSKWEKRSC
RRLCGDCGLA VKERRADMVS SCNCKFHWCC AVKCEQCRKS VTKYFCVKKE KRGGGIPRKK
ESKLKKKL
